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Database: UniProt/TrEMBL
Entry: A0A089YBK5_9PSED
LinkDB: A0A089YBK5_9PSED
Original site: A0A089YBK5_9PSED 
ID   A0A089YBK5_9PSED        Unreviewed;       397 AA.
AC   A0A089YBK5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   05-JUL-2017, entry version 17.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:AIR89168.1};
GN   ORFNames=LK03_07750 {ECO:0000313|EMBL:AIR89168.1};
OS   Pseudomonas cremoricolorata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR89168.1, ECO:0000313|Proteomes:UP000029493};
RN   [1] {ECO:0000313|EMBL:AIR89168.1, ECO:0000313|Proteomes:UP000029493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND07 {ECO:0000313|EMBL:AIR89168.1,
RC   ECO:0000313|Proteomes:UP000029493};
RA   Chan K.-G.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP009455; AIR89168.1; -; Genomic_DNA.
DR   RefSeq; WP_038411791.1; NZ_CP009455.1.
DR   EnsemblBacteria; AIR89168; AIR89168; LK03_07750.
DR   KEGG; psw:LK03_07750; -.
DR   KO; K02358; -.
DR   Proteomes; UP000029493; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029493};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AIR89168.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:AIR89168.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029493}.
FT   DOMAIN       10    207       Tr-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   397 AA;  43482 MW;  17CA834C2BF25601 CRC64;
     MAKEKFDRSL PHVNVGTIGH VDHGKTTLTA ALTRVCSEVF GSAVVEFDKI DSAPEEKARG
     ITINTAHVEY NSTIRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADL VDDAELLELV EMEVRDLLST YDFPGDDTPI IIGSARMALE
     GKDDNEMGTT AVKKLVETLD SYIPEPVRAI DQPFLMPIED VFSISGRGTV VTGRIERGIV
     RVQDPLEIVG LRDTTTTTCT GVEMFRKLLD EGRAGENCGV LLRGTKRDDV ERGQVLVKPG
     SVKPHTKFTA EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNCELPEG VEMVMPGDNI
     QMTVTLIKTI AMEDGLRFAI REGGRTVGAG VVAKIIE
//
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